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Volumn 109, Issue 25, 2012, Pages 9851-9856

Hydrophobic forces and the length limit of foldable protein domains

Author keywords

Folding funnel; Kinetics; Lattice model; Levinthal paradox

Indexed keywords

AMINO ACID; POLYPEPTIDE; WATER;

EID: 84862563497     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1207382109     Document Type: Article
Times cited : (31)

References (37)
  • 1
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen CB (1973) Principles that govern the folding of protein chains. Science 181:223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 2
    • 0025146274 scopus 로고
    • Implications of thermodynamics of protein folding for evolution of primary sequences
    • Shakhnovich EI, Gutin AM (1990) Implications of thermodynamics of protein folding for evolution of primary sequences. Nature 346:773-775.
    • (1990) Nature , vol.346 , pp. 773-775
    • Shakhnovich, E.I.1    Gutin, A.M.2
  • 3
    • 0001861319 scopus 로고
    • eds P Debrunner, JCM Tsibris, and E Munck (University of Illinois Press, Urbana)
    • Levinthal C (1969) Mossbauer Spectroscopy in Biological Systems, eds P Debrunner, JCM Tsibris, and E Munck (University of Illinois Press, Urbana), pp 22-24.
    • (1969) Mossbauer Spectroscopy in Biological Systems , pp. 22-24
    • Levinthal, C.1
  • 4
    • 0026320866 scopus 로고
    • The energy landscapes and motions of proteins
    • Frauenfelder H, Sligar SG, Wolynes PG (1991) The energy landscapes and motions of proteins. Science 254:1598-1603.
    • (1991) Science , vol.254 , pp. 1598-1603
    • Frauenfelder, H.1    Sligar, S.G.2    Wolynes, P.G.3
  • 6
    • 0029781355 scopus 로고    scopus 로고
    • The folding mechanism of larger model proteins: Role of native structure
    • Dinner AR, Sali A, Karplus M (1996) The folding mechanism of larger model proteins: Role of native structure. Proc Natl Acad Sci USA 93:8356-8361.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 8356-8361
    • Dinner, A.R.1    Sali, A.2    Karplus, M.3
  • 7
    • 0008863560 scopus 로고
    • Some factors in the interpretation of protein denaturation
    • Kauzmann W (1959) Some factors in the interpretation of protein denaturation. Adv Protein Chem 14:1-63.
    • (1959) Adv Protein Chem , vol.14 , pp. 1-63
    • Kauzmann, W.1
  • 8
    • 0014364651 scopus 로고
    • Protein denaturation
    • Tanford C (1968) Protein denaturation. Adv Protein Chem 23:121-282.
    • (1968) Adv Protein Chem , vol.23 , pp. 121-282
    • Tanford, C.1
  • 9
    • 0028802181 scopus 로고
    • Initial hydrophobic collapse in the folding of barstar
    • Agashe VR, Shastry MC, Udgaonkar JB (1995) Initial hydrophobic collapse in the folding of barstar. Nature 377:754-757.
    • (1995) Nature , vol.377 , pp. 754-757
    • Agashe, V.R.1    Shastry, M.C.2    Udgaonkar, J.B.3
  • 10
    • 77957752175 scopus 로고    scopus 로고
    • Evidence for initial non-specific polypeptide chain collapse during the refolding of the SH3 domain of PI3 kinase
    • Dasgupta A, Udgaonkar JB (2010) Evidence for initial non-specific polypeptide chain collapse during the refolding of the SH3 domain of PI3 kinase. J Mol Biol 403:430-445.
    • (2010) J Mol Biol , vol.403 , pp. 430-445
    • Dasgupta, A.1    Udgaonkar, J.B.2
  • 11
    • 0032561237 scopus 로고    scopus 로고
    • Pathways to a protein folding intermediate observed in a 1-microsecond simulation in aqueous solution
    • Duan Y, Kollman PA (1998) Pathways to a protein folding intermediate observed in a 1-microsecond simulation in aqueous solution. Science 282:740-744.
    • (1998) Science , vol.282 , pp. 740-744
    • Duan, Y.1    Kollman, P.A.2
  • 12
    • 0019443447 scopus 로고
    • The anatomy and taxonomy of protein structure
    • Richardson JS (1981) The anatomy and taxonomy of protein structure. Adv Protein Chem 34:167-339.
    • (1981) Adv Protein Chem , vol.34 , pp. 167-339
    • Richardson, J.S.1
  • 13
    • 0000327660 scopus 로고
    • Configuration and free energy of a polymer molecule with solvent interaction
    • Fisher ME, Hiley BJ (1961) Configuration and free energy of a polymer molecule with solvent interaction. J Chem Phys 34:1253-1267.
    • (1961) J Chem Phys , vol.34 , pp. 1253-1267
    • Fisher, M.E.1    Hiley, B.J.2
  • 14
    • 0001392074 scopus 로고
    • An evaluation of the number of hamiltonian paths
    • Orland HI, de Dominicis C (1985) An evaluation of the number of hamiltonian paths. J Physique Lett 46:353-357.
    • (1985) J Physique Lett , vol.46 , pp. 353-357
    • Orland, H.I.1    De Dominicis, C.2
  • 16
    • 0022423920 scopus 로고
    • Theory for the folding and stability of globular proteins
    • Dill KA (1985) Theory for the folding and stability of globular proteins. Biochemistry 24:1501-1509.
    • (1985) Biochemistry , vol.24 , pp. 1501-1509
    • Dill, K.A.1
  • 17
    • 0025343667 scopus 로고
    • Statistical distribution of hydrophobic residues along the length of protein chains. Implications for protein folding and evolution
    • White SH, Jacobs RE (1990) Statistical distribution of hydrophobic residues along the length of protein chains. Implications for protein folding and evolution. Biophys J 57:911-921.
    • (1990) Biophys J , vol.57 , pp. 911-921
    • White, S.H.1    Jacobs, R.E.2
  • 18
    • 0001510938 scopus 로고
    • Minimum energy compact structures of random sequences of heteropolymers
    • Camacho CJ, Thirumalai D (1993) Minimum energy compact structures of random sequences of heteropolymers. Phys Rev Lett 71:2505-2508.
    • (1993) Phys Rev Lett , vol.71 , pp. 2505-2508
    • Camacho, C.J.1    Thirumalai, D.2
  • 20
    • 0028950075 scopus 로고
    • Forces of tertiary structural organization in globular proteins
    • Yue K, Dill KA (1995) Forces of tertiary structural organization in globular proteins. Proc Natl Acad Sci USA 92:146-150.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 146-150
    • Yue, K.1    Dill, K.A.2
  • 21
    • 0027507346 scopus 로고
    • The evolution of proteins from random amino acid sequences 1. Evidence from the lengthwise distribution of amino acids in modern protein sequences
    • White SH, Jacobs RE (1993) The evolution of proteins from random amino acid sequences 1. Evidence from the lengthwise distribution of amino acids in modern protein sequences. J Mol Evol 36:79-95.
    • (1993) J Mol Evol , vol.36 , pp. 79-95
    • White, S.H.1    Jacobs, R.E.2
  • 22
    • 4243392673 scopus 로고
    • Proteins with selected sequences fold into unique native conformation
    • Shakhnovich EI (1994) Proteins with selected sequences fold into unique native conformation. Phys Rev Lett 72:3907-3910.
    • (1994) Phys Rev Lett , vol.72 , pp. 3907-3910
    • Shakhnovich, E.I.1
  • 23
    • 0016803266 scopus 로고
    • On the rate-determining step for helix propagation in the helix-coil transition of polypeptides in solution
    • Zana R (1975) on the rate-determining step for helix propagation in the helix-coil transition of polypeptides in solution. Biopolymers 14:2425-2428.
    • (1975) Biopolymers , vol.14 , pp. 2425-2428
    • Zana, R.1
  • 24
    • 0032502839 scopus 로고    scopus 로고
    • Contact order, transition state placement and the refolding rates of single domain proteins
    • Baker D
    • Plaxco KW, Simons KT, Baker D (1998) Contact order, transition state placement and the refolding rates of single domain proteins. J Mol Biol 277:985-994.
    • (1998) J Mol Biol , vol.277 , pp. 985-994
    • Plaxco, K.W.1    Simons, K.T.2
  • 25
    • 0042510944 scopus 로고    scopus 로고
    • Contact order revisited: Influence of protein size on the folding rate
    • Ivankov DN, et al. (2003) Contact order revisited: Influence of protein size on the folding rate. Protein Sci 12:2057-2062.
    • (2003) Protein Sci , vol.12 , pp. 2057-2062
    • Ivankov, D.N.1
  • 26
  • 27
    • 0029006062 scopus 로고
    • The multiplicity of domains in proteins
    • Doolittle RF (1995) The multiplicity of domains in proteins. Annu Rev Biochem 64:287-314.
    • (1995) Annu Rev Biochem , vol.64 , pp. 287-314
    • Doolittle, R.F.1
  • 28
    • 0028891784 scopus 로고
    • Identification and analysis of domains in proteins
    • Islam SA, Luo J, Sternberg MJ (1995) Identification and analysis of domains in proteins. Protein Eng 8:513-525.
    • (1995) Protein Eng , vol.8 , pp. 513-525
    • Islam, S.A.1    Luo, J.2    Sternberg, M.J.3
  • 29
    • 64049085201 scopus 로고    scopus 로고
    • Length variations amongst protein domain superfamilies and consequences on structure and function
    • Sandhya S, et al. (2009) Length variations amongst protein domain superfamilies and consequences on structure and function. PLoS One 4(3):e4981.
    • (2009) PLoS One , vol.4 , Issue.3
    • Sandhya, S.1
  • 31
    • 84986512474 scopus 로고
    • Charmm - A program for macromolecular energy, minimization, and dynamics calculations
    • Brooks BR, et al. (1983) Charmm - A program for macromolecular energy, minimization, and dynamics calculations. J Comput Chem 4:187-217.
    • (1983) J Comput Chem , vol.4 , pp. 187-217
    • Brooks, B.R.1
  • 32
    • 0037032225 scopus 로고    scopus 로고
    • Smaller and faster: The 20-residue Trp-cage protein folds in 4 μs
    • Qiu LL, Pabit SA, Roitberg AE, Hagen SJ (2002) Smaller and faster: The 20-residue Trp-cage protein folds in 4 μs. J Am Chem Soc 124:12952-12953.
    • (2002) J Am Chem Soc , vol.124 , pp. 12952-12953
    • Qiu, L.L.1    Pabit, S.A.2    Roitberg, A.E.3    Hagen, S.J.4
  • 33
    • 0028928486 scopus 로고
    • Biomolecular folding in vacuo!!!(?)
    • Wolynes PG (1995) Biomolecular folding in vacuo!!!(?). Proc Natl Acad Sci USA 92:2426-2427.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 2426-2427
    • Wolynes, P.G.1
  • 34
    • 0014691177 scopus 로고
    • Natural selection and the complexity of the gene
    • Salisbury FB (1969) Natural selection and the complexity of the gene. Nature 224:342-343.
    • (1969) Nature , vol.224 , pp. 342-343
    • Salisbury, F.B.1
  • 35
    • 0014935646 scopus 로고
    • Natural selection and the concept of a protein space
    • Smith JM (1970) Natural selection and the concept of a protein space. Nature 225:563-564.
    • (1970) Nature , vol.225 , pp. 563-564
    • Smith, J.M.1
  • 36
    • 0030989408 scopus 로고    scopus 로고
    • Three-dimensional domain duplication, swapping and stealing
    • Heringa J, Taylor WR (1997) Three-dimensional domain duplication, swapping and stealing. Curr Opin Struct Biol 7:416-421.
    • (1997) Curr Opin Struct Biol , vol.7 , pp. 416-421
    • Heringa, J.1    Taylor, W.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.